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Information on EC 5.6.1.5 - proteasome ATPase

for references in articles please use BRENDA:EC5.6.1.5
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EC Tree
IUBMB Comments
Belongs to the AAA-type superfamily and, like EC 5.6.1.4 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
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This record set is specific for:
UNIPROT: Q04019
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Word Map
  • 5.6.1.5
  • atpases
  • ubiquitin-proteasome
  • subcomplexes
  • misfolded
  • hexameric
  • polyubiquitinated
  • disassembly
  • hslu
  • ubiquitin-dependent
  • non-atpase
  • ubiquitin-like
  • er-associated
  • multisubunit
  • deubiquitinase
  • reticulum-associated
  • proteotoxic
  • retrotranslocation
  • proteasome-mediated
  • escrts
  • deubiquitylating
  • valosin-containing
  • immunoproteasome
  • katanin
  • proteasome-associated
  • zellweger
  • escrt-iii
  • spastin
  • medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
+
=
+
+
unfolded polypeptide
Synonyms
aaa atpase, pa700, 19s regulatory particle, 19s proteasome, hslvu, tbp-1, 19s rp, rpt2a, psmc5, 26s-proteasome, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
regulatory particle 5a
AAA-ATPase of the proteasome regulatory particle
regulatory particle 5b
AAA-ATPase of the proteasome regulatory particle
RP triphosphatase
-
-
-
-
RP triple-A protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-degrading)
Belongs to the AAA-type superfamily and, like EC 5.6.1.4 (minus-end-directed kinesin ATPase), is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome. Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + polypeptide
ADP + phosphate + unfolded polypeptide
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
YM80_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
206
0
23194
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gallois, J.L.; Guyon-Debast, A.; Lecureuil, A.; Vezon, D.; Carpentier, V.; Bonhomme, S.; Guerche, P.
The Arabidopsis proteasome RPT5 subunits are essential for gametophyte development and show accession-dependent redundancy
Plant Cell
21
442-459
2009
Arabidopsis thaliana (Q04019), Arabidopsis thaliana
Manually annotated by BRENDA team